Associated Papers
Structures of the PKC-iota kinase domain in its ATP-bound and apo forms reveal defined structures of residues 533-551 in the C-terminal tail and their roles in ATP binding.
Takimura T et al.
Acta Crystallographica. Section D, Biological Crystallography, 2010
Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif.
Messerschmidt A et al.
Journal of Molecular Biology, 2005
Select a paper to view details